Cyclic AMP-dependent protein kinase phosphorylates and inactivates the yeast transcriptional activator ADR1

Cell. 1989 Feb 10;56(3):409-19. doi: 10.1016/0092-8674(89)90244-4.


It has been proposed in several eukaryotic systems that the regulation of gene transcription involves phosphorylation of specific transcription factors. We report here that the yeast transcriptional activator ADR1 is phosphorylated in vitro by cyclic AMP-dependent protein kinase and that mutations which enhance the ability of ADR1 to activate ADH2 expression decrease ADR1 phosphorylation. We also show that increased kinase activity in vivo inhibits ADH2 expression in an ADR1 allele-specific manner. Our data suggest that glucose repression of ADH2 is in part mediated through a cAMP-dependent phosphorylation-inactivation of the ADR1 regulatory protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aldehyde Dehydrogenase / genetics
  • Amino Acid Sequence
  • DNA-Binding Proteins*
  • Escherichia coli / genetics
  • Fungal Proteins / antagonists & inhibitors*
  • Fungal Proteins / genetics
  • Genes
  • Genes, Fungal
  • Molecular Sequence Data
  • Mutation
  • Peptide Mapping
  • Phosphorylation
  • Plasmids
  • Protein Kinases / metabolism*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors*


  • ADR1 protein, S cerevisiae
  • DNA-Binding Proteins
  • Fungal Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Aldehyde Dehydrogenase
  • Protein Kinases